ID   E3NUP4_CAERE            Unreviewed;       500 AA.
AC   E3NUP4;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   27-MAR-2024, entry version 66.
DE   RecName: Full=thioredoxin-disulfide reductase {ECO:0000256|ARBA:ARBA00012610};
DE            EC=1.8.1.9 {ECO:0000256|ARBA:ARBA00012610};
GN   ORFNames=CRE_26919 {ECO:0000313|EMBL:EFO96052.1};
OS   Caenorhabditis remanei (Caenorhabditis vulgaris).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=31234 {ECO:0000313|Proteomes:UP000008281};
RN   [1] {ECO:0000313|Proteomes:UP000008281}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PB4641 {ECO:0000313|Proteomes:UP000008281};
RG   Caenorhabditis remanei Sequencing Consortium;
RA   Wilson R.K.;
RT   "PCAP assembly of the Caenorhabditis remanei genome.";
RL   Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC       oxidoreductase family. {ECO:0000256|ARBA:ARBA00007532,
CC       ECO:0000256|RuleBase:RU003691}.
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DR   EMBL; DS270629; EFO96052.1; -; Genomic_DNA.
DR   RefSeq; XP_003087877.1; XM_003087829.1.
DR   AlphaFoldDB; E3NUP4; -.
DR   STRING; 31234.E3NUP4; -.
DR   EnsemblMetazoa; CRE26919.1; CRE26919.1; WBGene00075508.
DR   eggNOG; KOG4716; Eukaryota.
DR   HOGENOM; CLU_016755_2_4_1; -.
DR   InParanoid; E3NUP4; -.
DR   OMA; DFALFTI; -.
DR   OrthoDB; 5473641at2759; -.
DR   Proteomes; UP000008281; Unassembled WGS sequence.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016668; F:oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor; IEA:InterPro.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR   Gene3D; 3.30.390.30; -; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR   InterPro; IPR046952; GSHR/TRXR-like.
DR   InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR   InterPro; IPR012999; Pyr_OxRdtase_I_AS.
DR   PANTHER; PTHR42737; GLUTATHIONE REDUCTASE; 1.
DR   PANTHER; PTHR42737:SF8; THIOREDOXIN REDUCTASE 1; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   Pfam; PF02852; Pyr_redox_dim; 1.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00411; PNDRDTASEI.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
DR   PROSITE; PS00076; PYRIDINE_REDOX_1; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|RuleBase:RU003691};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW   ECO:0000256|RuleBase:RU003691};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU003691};
KW   Redox-active center {ECO:0000256|ARBA:ARBA00023284,
KW   ECO:0000256|RuleBase:RU003691};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008281}.
FT   DOMAIN          161..366
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          371..483
FT                   /note="Pyridine nucleotide-disulphide oxidoreductase
FT                   dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF02852"
FT   REGION          1..50
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..21
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   500 AA;  55091 MW;  D921599665383DC1 CRC64;
     MVFFSVTAPA NQSTSDTPSM GAVASGMPPP KRPAPAESPT LPDERNVDEP GIPLKEALKE
     ANNAKIAVFY SQNTSDEEKQ ILEIEAILKA LKDPADVEKP LEIPDVQRIR VSSASKKAIQ
     YLTLHNSWPL IYIKGNAVGG LKELQALKKD YLKEWLRDHT YDLIVIGGGS GGLAAAKEAA
     RLGKKVACLD FVKPSPQGTT WGLGGTCVNV GCIPKKLMHQ ASLLGHSIHD AQKFGWKLEG
     KPEHQWGHLR DSVQDHIASL NWGYRVQLRE KTVTYINSYG EFTGPFEISA TNKKKKVEKI
     TADRFLIATG LRPKYPDFPG VKEYTITSDD LFQLPYSPGK TLCVGASYVS LECAGFLHGL
     GFDVTTEYDQ IPTTVFTPLE YGCCGLAEED AVKKYGKENI IIYHNVFNPL EYTISERMDK
     DHCYLKLICL RNEEEKVVGF HILTPNAGEI TQGFGIALKL SAKKADFDRL IGIHPTVAES
     FTTLTLEKKD GDEELQASGC
//